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Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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Each human somatic cell contains 6 billion base pairs of DNA. Each base pair is 0.34 nm long, meaning each diploid cell contains a staggering 2 meters of DNA. This long DNA strand is packed inside a nucleus measuring only 10-20 microns in diameter with the help of specialized DNA-binding proteins called histones. Together they form a compact DNA-protein complex called chromatin. The chromatin is further compacted into higher-order structures. The highest level of compaction is achieved during...
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DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
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Related Experiment Video

Updated: Nov 26, 2025

Author Spotlight: Unraveling the Dynamics of Eukaryotic DNA Replication Through Single-Molecule Visualization
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Purified Smc5/6 Complex Exhibits DNA Substrate Recognition and Compaction.

Pilar Gutierrez-Escribano1, Silvia Hormeño2, Julene Madariaga-Marcos2

  • 1Cell Cycle Group, MRC London Institute of Medical Sciences (LMS), Du Cane Road, London W12 0NN, UK.

Molecular Cell
|December 10, 2020
PubMed
Summary

The Smc5/6 complex, crucial for chromosome organization, binds and compacts DNA by stabilizing plectonemes. This ATP-dependent mechanism reveals new insights into DNA topology modulation.

Keywords:
DNA compactionDNA substrate recognitionSmc5/6 holocomplexSmc5/6 purificationelectron mmicroscopymagnetic tweezersplectoneme stabilisationsingle-molecule

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Eukaryotic structural maintenance of chromosome (SMC) complexes, including cohesin, condensin, and Smc5/6, are essential for chromosome organization and dynamics.
  • The precise mechanism of action and DNA interactions of the Smc5/6 complex remain largely uncharacterized.

Purpose of the Study:

  • To purify and characterize the biochemical and biophysical activities of the budding yeast Smc5/6 holocomplex.
  • To elucidate the DNA binding properties and functional mechanisms of Smc5/6.

Main Methods:

  • Purification of the Smc5/6 holocomplex from budding yeast.
  • Biochemical assays for ATP hydrolysis and SUMO E3 ligase activity.
  • Single-molecule assays to analyze DNA binding and compaction dynamics.

Main Results:

  • Purified Smc5/6 exhibits DNA-dependent ATP hydrolysis and SUMO E3 ligase activity.
  • Smc5/6 binds DNA topologically, with a preference for supercoiled and catenated DNA.
  • Smc5/6 stabilizes DNA plectonemes and compacts DNA in an ATP-dependent manner, recognizing juxtaposed helices.

Conclusions:

  • The Smc5/6 complex plays a role in modulating DNA topology through plectoneme stabilization and local compaction.
  • Smc5/6's ability to recognize and interact with complex DNA structures highlights its importance in chromosome organization.